PLK4_MOUSE
ID PLK4_MOUSE Reviewed; 925 AA.
AC Q64702; Q3UVA3; Q6PEP6; Q78EG6; Q80UT6; Q8R0I5; Q9CVR6; Q9CVU6;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Serine/threonine-protein kinase PLK4 {ECO:0000305};
DE EC=2.7.11.21 {ECO:0000250|UniProtKB:O00444};
DE AltName: Full=Polo-like kinase 4;
DE Short=PLK-4;
DE AltName: Full=Serine/threonine-protein kinase 18;
DE AltName: Full=Serine/threonine-protein kinase Sak;
GN Name=Plk4 {ECO:0000312|MGI:MGI:101783}; Synonyms=Sak, Stk18;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC STRAIN=DBA/2J; TISSUE=Lymphoma;
RX PubMed=8022793; DOI=10.1073/pnas.91.14.6388;
RA Fode C., Motro B., Yousefi S., Heffernan M., Dennis J.W.;
RT "Sak, a murine protein-serine/threonine kinase that is related to the
RT Drosophila polo kinase and involved in cell proliferation.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6388-6392(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone, Embryo, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP UBIQUITINATION.
RX PubMed=8756623; DOI=10.1128/mcb.16.9.4665;
RA Fode C., Binkert C., Dennis J.W.;
RT "Constitutive expression of murine Sak-a suppresses cell growth and induces
RT multinucleation.";
RL Mol. Cell. Biol. 16:4665-4672(1996).
RN [6]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=11301255; DOI=10.1016/s0960-9822(01)00117-8;
RA Hudson J.W., Kozarova A., Cheung P., Macmillan J.C., Swallow C.J.,
RA Cross J.C., Dennis J.W.;
RT "Late mitotic failure in mice lacking Sak, a polo-like kinase.";
RL Curr. Biol. 11:441-446(2001).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=16025114; DOI=10.1038/ng1605;
RA Ko M.A., Rosario C.O., Hudson J.W., Kulkarni S., Pollett A., Dennis J.W.,
RA Swallow C.J.;
RT "Plk4 haploinsufficiency causes mitotic infidelity and carcinogenesis.";
RL Nat. Genet. 37:883-888(2005).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-170.
RX PubMed=17891141; DOI=10.1038/ncb1633;
RA Martindill D.M.J., Risebro C.A., Smart N., Franco-Viseras Mdel M.,
RA Rosario C.O., Swallow C.J., Dennis J.W., Riley P.R.;
RT "Nucleolar release of Hand1 acts as a molecular switch to determine cell
RT fate.";
RL Nat. Cell Biol. 9:1131-1141(2007).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24240477; DOI=10.1038/ncb2880;
RA Zhao H., Zhu L., Zhu Y., Cao J., Li S., Huang Q., Xu T., Huang X., Yan X.,
RA Zhu X.;
RT "The Cep63 paralogue Deup1 enables massive de novo centriole biogenesis for
RT vertebrate multiciliogenesis.";
RL Nat. Cell Biol. 15:1434-1444(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 839-925, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12352953; DOI=10.1038/nsb848;
RA Leung G.C., Hudson J.W., Kozarova A., Davidson A., Dennis J.W., Sicheri F.;
RT "The Sak polo-box comprises a structural domain sufficient for mitotic
RT subcellular localization.";
RL Nat. Struct. Biol. 9:719-724(2002).
CC -!- FUNCTION: Serine/threonine-protein kinase that plays a central role in
CC centriole duplication. Able to trigger procentriole formation on the
CC surface of the parental centriole cylinder, leading to the recruitment
CC of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110,
CC CEP135 and gamma-tubulin. When overexpressed, it is able to induce
CC centrosome amplification through the simultaneous generation of
CC multiple procentrioles adjoining each parental centriole during S
CC phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition,
CC leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central
CC role in centriole replication suggests a possible role in
CC tumorigenesis, centrosome aberrations being frequently observed in
CC tumors. Phosphorylates CDC25C and CHEK2. Also involved in deuterosome-
CC mediated centriole amplification in multiciliated that can generate
CC more than 100 centrioles. Also involved in trophoblast differentiation
CC by phosphorylating HAND1, leading to disrupt the interaction between
CC HAND1 and MDFIC and activate HAND1. Required for the recruitment of
CC STIL to the centriole and for STIL-mediated centriole amplification (By
CC similarity). Phosphorylates CEP131 at 'Ser-78' and PCM1 at 'Ser-372'
CC which is essential for proper organization and integrity of centriolar
CC satellites (By similarity). {ECO:0000250|UniProtKB:O00444,
CC ECO:0000269|PubMed:17891141, ECO:0000269|PubMed:24240477}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.21;
CC -!- SUBUNIT: Homodimer (PubMed:12352953). Interacts with CEP152 (via N-
CC terminus) (By similarity). Interacts with CEP78; this interaction may
CC be important for proper PLK4 localization to the centriole and PLK4-
CC induced overduplication of centrioles (By similarity). Interacts with
CC CEP131 (By similarity). Interacts simultaneously with TENT5C and
CC CEP192. Interacts with TENT5C; this interaction leads to the TENT5C
CC recruitment in the centrosome (By similarity).
CC {ECO:0000250|UniProtKB:O00444, ECO:0000269|PubMed:12352953}.
CC -!- INTERACTION:
CC Q64702; Q64702: Plk4; NbExp=4; IntAct=EBI-2552433, EBI-2552433;
CC Q64702; Q8WWL7: CCNB3; Xeno; NbExp=4; IntAct=EBI-2552433, EBI-767764;
CC Q64702; P02686-1: MBP; Xeno; NbExp=2; IntAct=EBI-2552433, EBI-7056012;
CC Q64702; P03772; Xeno; NbExp=2; IntAct=EBI-2552433, EBI-4478820;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:11301255}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:11301255}. Cleavage furrow
CC {ECO:0000269|PubMed:11301255}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:O00444}.
CC Note=Associates with centrioles throughout the cell cycle. According to
CC PubMed:11301255, it localizes to the nucleolus during G2, to the
CC centrosomes in G2/M, and to the cleavage furrow during cytokinesis.
CC Component of the deuterosome, a structure that promotes de novo
CC centriole amplification in multiciliated cells that can generate more
CC than 100 centrioles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Sak-a;
CC IsoId=Q64702-1; Sequence=Displayed;
CC Name=2; Synonyms=Sak-b;
CC IsoId=Q64702-2; Sequence=VSP_011369, VSP_011370;
CC Name=3;
CC IsoId=Q64702-3; Sequence=VSP_011371;
CC -!- TISSUE SPECIFICITY: expressed in tissues associated with mitotic and
CC meiotic cell division. Highly expressed in testis.
CC {ECO:0000269|PubMed:8022793}.
CC -!- DOMAIN: Cryptic POLO box 1 (CPB1) and Cryptic POLO box 2 (CPB2) domains
CC can simultaneously bind to both TENT5C and CEP192.
CC {ECO:0000250|UniProtKB:O00444}.
CC -!- PTM: Ubiquitinated; leading to its degradation by the proteasome.
CC {ECO:0000269|PubMed:8756623}.
CC -!- PTM: Tyrosine-phosphorylated by TEC. {ECO:0000250}.
CC -!- PTM: Acetylation by KAT2A and KAT2B impairs kinase activity by shifting
CC the kinase to an inactive conformation. {ECO:0000250|UniProtKB:O00444}.
CC -!- DISRUPTION PHENOTYPE: Death during embryogenesis. Embryos arrest after
CC gastrulation at E7.5, with a marked increase in mitotic and apoptotic
CC cells. Heterozygous mice are viable but show increased liver and lung
CC cancers in elderly mice. Defects in heterozygous mice are associated
CC with progressive cell cycle delays, increased spindle irregularities
CC and accelerated hepatocellular carcinogenesis, probably due to
CC increased centrosomal amplification, multipolar spindle formation and
CC aneuploidy. The incidence of spontaneous. {ECO:0000269|PubMed:11301255,
CC ECO:0000269|PubMed:16025114}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU01328,
CC ECO:0000255|PROSITE-ProRule:PRU01329}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH51483.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L29479; AAC37648.1; -; mRNA.
DR EMBL; L29480; AAC37649.1; -; mRNA.
DR EMBL; AK006459; BAB24599.1; -; mRNA.
DR EMBL; AK006827; BAB24759.1; -; mRNA.
DR EMBL; AK137080; BAE23231.1; -; mRNA.
DR EMBL; AK137471; BAE23367.1; -; mRNA.
DR EMBL; CH466530; EDL35140.1; -; Genomic_DNA.
DR EMBL; CH466530; EDL35142.1; -; Genomic_DNA.
DR EMBL; BC026785; AAH26785.1; -; mRNA.
DR EMBL; BC051483; AAH51483.1; ALT_INIT; mRNA.
DR EMBL; BC057940; AAH57940.1; -; mRNA.
DR CCDS; CCDS17328.1; -. [Q64702-1]
DR CCDS; CCDS57210.1; -. [Q64702-3]
DR PIR; A55748; A55748.
DR RefSeq; NP_035625.2; NM_011495.2. [Q64702-1]
DR RefSeq; NP_775261.2; NM_173169.2. [Q64702-3]
DR PDB; 1MBY; X-ray; 2.00 A; A/B=839-925.
DR PDBsum; 1MBY; -.
DR AlphaFoldDB; Q64702; -.
DR BMRB; Q64702; -.
DR SMR; Q64702; -.
DR BioGRID; 203545; 17.
DR ComplexPortal; CPX-1160; CEP152-PLK4 complex.
DR ComplexPortal; CPX-1298; CEP192-PLK4 complex.
DR DIP; DIP-42244N; -.
DR IntAct; Q64702; 8.
DR MINT; Q64702; -.
DR STRING; 10090.ENSMUSP00000026858; -.
DR iPTMnet; Q64702; -.
DR PhosphoSitePlus; Q64702; -.
DR PaxDb; Q64702; -.
DR PRIDE; Q64702; -.
DR ProteomicsDB; 288252; -. [Q64702-1]
DR ProteomicsDB; 288253; -. [Q64702-2]
DR ProteomicsDB; 288254; -. [Q64702-3]
DR Antibodypedia; 26934; 223 antibodies from 35 providers.
DR DNASU; 20873; -.
DR Ensembl; ENSMUST00000026858; ENSMUSP00000026858; ENSMUSG00000025758. [Q64702-1]
DR Ensembl; ENSMUST00000203295; ENSMUSP00000145277; ENSMUSG00000025758. [Q64702-3]
DR GeneID; 20873; -.
DR KEGG; mmu:20873; -.
DR UCSC; uc008pbm.1; mouse. [Q64702-2]
DR UCSC; uc008pbo.1; mouse. [Q64702-1]
DR UCSC; uc012cpc.1; mouse. [Q64702-3]
DR CTD; 10733; -.
DR MGI; MGI:101783; Plk4.
DR VEuPathDB; HostDB:ENSMUSG00000025758; -.
DR eggNOG; KOG0575; Eukaryota.
DR GeneTree; ENSGT00940000156316; -.
DR HOGENOM; CLU_008726_1_0_1; -.
DR InParanoid; Q64702; -.
DR OMA; HSSWSEP; -.
DR OrthoDB; 507604at2759; -.
DR PhylomeDB; Q64702; -.
DR TreeFam; TF101090; -.
DR BRENDA; 2.7.11.21; 3474.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 20873; 14 hits in 32 CRISPR screens.
DR EvolutionaryTrace; Q64702; -.
DR PRO; PR:Q64702; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q64702; protein.
DR Bgee; ENSMUSG00000025758; Expressed in animal zygote and 67 other tissues.
DR ExpressionAtlas; Q64702; baseline and differential.
DR Genevisible; Q64702; MM.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098536; C:deuterosome; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0120098; C:procentriole; ISO:MGI.
DR GO; GO:0120099; C:procentriole replication complex; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0001741; C:XY body; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0098535; P:de novo centriole assembly involved in multi-ciliated epithelial cell differentiation; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0046601; P:positive regulation of centriole replication; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IMP:UniProtKB.
DR CDD; cd13114; POLO_box_Plk4_1; 1.
DR CDD; cd13115; POLO_box_Plk4_2; 1.
DR CDD; cd13116; POLO_box_Plk4_3; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033700; Plk4.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR033699; POLO_box_Plk4_1.
DR InterPro; IPR033698; POLO_box_Plk4_2.
DR InterPro; IPR033696; POLO_box_Plk4_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR24345:SF89; PTHR24345:SF89; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF18190; Plk4_PB1; 1.
DR Pfam; PF18409; Plk4_PB2; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51984; CPB1; 1.
DR PROSITE; PS51985; CPB2; 1.
DR PROSITE; PS50078; POLO_BOX; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Cytoskeleton; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation.
FT CHAIN 1..925
FT /note="Serine/threonine-protein kinase PLK4"
FT /id="PRO_0000086568"
FT DOMAIN 12..265
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 547..660
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT DOMAIN 661..774
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT DOMAIN 847..911
FT /note="POLO box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 262..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 45
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00444"
FT MOD_RES 46
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00444"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00444"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00444"
FT VAR_SEQ 417..464
FT /note="SSNHHCLGKTPFPFADQTPQMEMVQQWFGNLQMNAHLGETNEHHTVSP ->
FT RYSPTKSNVNVLTSLNTKQPIVKDLLKDRIMTEQYKDNLLNLLNKFDR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:8022793"
FT /id="VSP_011369"
FT VAR_SEQ 465..925
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8022793"
FT /id="VSP_011370"
FT VAR_SEQ 580..606
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011371"
FT MUTAGEN 170
FT /note="T->D: Activating mutant."
FT /evidence="ECO:0000269|PubMed:17891141"
FT CONFLICT 201
FT /note="F -> S (in Ref. 1; AAC37648/AAC37649)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="D -> E (in Ref. 2; BAB24759)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="M -> V (in Ref. 2; BAB24599)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="G -> D (in Ref. 3; AAH26785/AAH57940)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="A -> E (in Ref. 3; AAH26785)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="D -> N (in Ref. 3; AAH26785/AAH57940)"
FT /evidence="ECO:0000305"
FT STRAND 848..855
FT /evidence="ECO:0007829|PDB:1MBY"
FT STRAND 857..866
FT /evidence="ECO:0007829|PDB:1MBY"
FT STRAND 871..884
FT /evidence="ECO:0007829|PDB:1MBY"
FT STRAND 890..894
FT /evidence="ECO:0007829|PDB:1MBY"
FT HELIX 901..907
FT /evidence="ECO:0007829|PDB:1MBY"
FT TURN 908..910
FT /evidence="ECO:0007829|PDB:1MBY"
FT STRAND 913..917
FT /evidence="ECO:0007829|PDB:1MBY"
SQ SEQUENCE 925 AA; 103746 MW; F28A64ED24D9C801 CRC64;
MAACIGERIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK AGMVQRVQNE
VKIHCQLKHP SVLELYNYFE DNNYVYLVLE MCHNGEMNRY LKNRMKPFSE REARHFMHQI
ITGMLYLHSH GILHRDLTLS NILLTRNMNI KIADFGLATQ LNMPHEKHYT LCGTPNYISP
EIATRSAHGL ESDIWSLGCM FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PAFLSREAQD
LIHQLLRRNP ADRLSLSSVL DHPFMSRNPS PKSKDVGTVE DSMDSGHATL STTITASSGT
SLSGSLLDRR LLVGQPLPNK ITVFQKNKNS SDFSSGDGSN FCTQWGNPEQ EANSRGRGRV
IEDAEERPHS RYLRRAHSSD RASPSNQSRA KTYSVERCHS VEMLSKPRRS LDENQHSSNH
HCLGKTPFPF ADQTPQMEMV QQWFGNLQMN AHLGETNEHH TVSPNRDFQD YPDLQDTLRN
AWTDTRASKN ADTSANVHAV KQLSAMKYMS AHHHKPEVMP QEPGLHPHSE QSKNRSMEST
LGYQKPTLRS ITSPLIAHRL KPIRQKTKKA VVSILDSEEV CVELLRECAS EGYVKEVLQI
SSDGTMITVY YPNDGRGFPL ADRPPLPTDN ISRYSFDNLP EKYWRKYQYA SRFIQLVRSK
TPKITYFTRY AKCILMENSP GADFEVWFYD GAKIHKTENL IHIIEKTGIS YNLKNENEVT
SLKEEVKVYM DHANEGHRIC LSLESVISEE EKRSRGSSFF PIIVGRKPGN TSSPKALSAP
PVDPSCCKGE QASASRLSVN SAAFPTQSPG LSPSTVTVEG LGHTATATGT GVSSSLPKSA
QLLKSVFVKN VGWATQLTSG AVWVQFNDGS QLVVQAGVSS ISYTSPDGQT TRYGENEKLP
EYIKQKLQCL SSILLMFSNP TPNFQ
